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Q87T81 (FPG_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formamidopyrimidine-DNA glycosylase

Short name=Fapy-DNA glycosylase
EC=3.2.2.23
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM
Short name=AP lyase MutM
EC=4.2.99.18
Gene names
Name:mutM
Synonyms:fpg
Ordered Locus Names:VP0189
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates By similarity. HAMAP-Rule MF_00103

Catalytic activity

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. HAMAP-Rule MF_00103

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_00103

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103

Sequence similarities

Belongs to the FPG family.

Contains 1 FPG-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 269268Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000170883

Regions

Zinc finger235 – 26935FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site571Proton donor; for beta-elimination activity By similarity
Active site2591Proton donor; for delta-elimination activity By similarity
Binding site901DNA By similarity
Binding site1091DNA By similarity
Binding site1501DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87T81 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 77A1CB9CEF07E8C6

FASTA26930,096
        10         20         30         40         50         60 
MPELPEVEVS RMGISPHMVG QTIKAFVFRT PKLRWDIPQE LKLLEGQVIR NIRRRAKYLL 

        70         80         90        100        110        120 
IDTDQGTAIV HLGMSGSLRV LDADFPAAKH DHVDLKLTNG KVLRYNDPRR FGAWLWCAPG 

       130        140        150        160        170        180 
ESHAVLEHMG PEPLTDAFNS EYIADKAQGK RVAVKQFIMD NKVVVGVGNI YANESLFKSR 

       190        200        210        220        230        240 
ILPTRQAGQV TPQEWVLLVE NIKATLKIAI NQGGTTLKDF AQADGKPGYF AQELLVYGKA 

       250        260 
GEPCPECGEP LQELKIGQRN TFFCNECQQ 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC58452.1.
RefSeqNP_796568.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87T81.
SMRQ87T81. Positions 2-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP0189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC58452; BAC58452; BAC58452.
GeneID1187656.
KEGGvpa:VP0189.
PATRIC20138612. VBIVibPar50997_0181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-200-MONOMER.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsTIGR00577. fpg. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPG_VIBPA
AccessionPrimary (citable) accession number: Q87T81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families